|PROSITE documentation PDOC00487 [for PROSITE entry PS51663]|
Stathmin  (from the Greek 'stathmos' which means relay), is an ubiquitous intracellular protein, present in a variety of phosphorylated forms and which is involved in the regulation of the microtubule (MT) filament system by destabilizing microtubules. It prevents assembly and promotes disassembly of microtubules.
Stathmin belongs to a family that also includes:
These proteins possess a stathmin-like domain (SLD) with various N-terminal extensions. SLD is a highly conserved domain of 149 amino acid residues. Structurally, it consists of an N-terminal domain of about 45 residues followed by a 78 residue α-helical domain consisting of a heptad repeat coiled coil structure and a C-terminal domain of 25 residues (see <PDB:1SA0>) . The SLD binds two tubulins arranged longitudinally, head-to-tail, in protofilament-like complexes.
As signatures for proteins of the stathmin family, we selected a conserved decapeptide which ends with the first three residues of the coiled coil domain and a second pattern that corresponds to part of the central region of the coiled coil. We also developed a profile that covers the entire SLD domain.Last update:
January 2013 / Text revised; profile added.
PROSITE methods (with tools and information) covered by this documentation:
|Title||Stathmin: a relay phosphoprotein for multiple signal transduction?|
|Source||Trends Biochem. Sci. 16:301-305(1991).|
|2||Authors||Ozon S. Byk T. Sobel A.|
|Title||SCLIP: a novel SCG10-like protein of the stathmin family expressed in the nervous system.|
|Source||J. Neurochem. 70:2386-2396(1998).|
|3||Authors||Ozon S. Maucuer A. Sobel A.|
|Title||The stathmin family -- molecular and biological characterization of novel mammalian proteins expressed in the nervous system.|
|Source||Eur. J. Biochem. 248:794-806(1997).|
|4||Authors||Ravelli R.B.G. Gigant B. Curmi P.A. Jourdain I. Lachkar S. Sobel A. Knossow M.|
|Title||Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain.|